1ol0
From Proteopedia
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| - | + | ==CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH== | |
| - | + | <StructureSection load='1ol0' size='340' side='right' caption='[[1ol0]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1ol0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OL0 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a8j|1a8j]], [[1aj7|1aj7]], [[1ar2|1ar2]], [[1b6d|1b6d]], [[1bm3|1bm3]], [[1bre|1bre]], [[1bww|1bww]], [[1cmo|1cmo]], [[1ek3|1ek3]], [[1epf|1epf]], [[1fig|1fig]], [[1ie5|1ie5]], [[1igm|1igm]], [[1ikf|1ikf]], [[1ind|1ind]], [[1ine|1ine]], [[1ivl|1ivl]], [[1jgl|1jgl]], [[1jvk|1jvk]], [[1koa|1koa]], [[1ksr|1ksr]], [[1lve|1lve]], [[1mcb|1mcb]], [[1mcc|1mcc]], [[1mcd|1mcd]], [[1mce|1mce]], [[1mcf|1mcf]], [[1mch|1mch]], [[1mci|1mci]], [[1mcj|1mcj]], [[1mck|1mck]], [[1mcl|1mcl]], [[1mcn|1mcn]], [[1mco|1mco]], [[1mcp|1mcp]], [[1mcq|1mcq]], [[1mcr|1mcr]], [[1mcs|1mcs]], [[1mcw|1mcw]], [[1rei|1rei]], [[1vkx|1vkx]], [[1wit|1wit]], [[1wiu|1wiu]], [[2dl2|2dl2]], [[2dli|2dli]], [[2fb4|2fb4]], [[2ig2|2ig2]], [[2imm|2imm]], [[2imn|2imn]], [[2loi|2loi]], [[2mcg|2mcg]], [[2mcp|2mcp]], [[2rcs|2rcs]], [[3mcg|3mcg]], [[5lve|5lve]], [[7fab|7fab]], [[8fab|8fab]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ol0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ol0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ol0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ol0 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/1ol0_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The variable domain of dromedary immunoglobulins comprises only the heavy chain and is missing the light-chain variable domain. This single domain is sufficient for antigen recognition and binding-half that required by other mammals. Human antibody-VHs have previously been camelized to be soluble stable fragments that retain antigen binding. Such engineered VHH are of interest in drug development, since they are nonimmunogenic, and in other biotechnology applications. We present the structure of a camelized human antibody fragment (cVH), which is a competitive and reversible inhibitor of the NS3 serine protease of the hepatitis C virus (HCV). In solution, this cVH undergoes a concentration-dependent monomer-dimer equilibrium. The structure confirms the minimum mutational requirements of the VL-binding face. The fragment also suggests a means by which the observed dimerization occurs, highlighting the importance of the composition of the CDR3 in maintaining a truly camelized VH. | ||
| - | + | Crystal structure of a human VH: requirements for maintaining a monomeric fragment.,Dottorini T, Vaughan CK, Walsh MA, LoSurdo P, Sollazzo M Biochemistry. 2004 Jan 27;43(3):622-8. PMID:14730966<ref>PMID:14730966</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Dottorini, T.]] | [[Category: Dottorini, T.]] | ||
Revision as of 10:19, 3 October 2014
CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH
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